Fig. 1

Secondary structure prediction and three-dimensional (3-D) structure prediction of the four Hpa1. a Secondary structures prediction for four Hpa1 using NPS (https://npsa-prabi.ibcp.fr/cgi-bin/secpred_hnn.pl). Secondary structure predictions indicated the presence of α-helix (h), extended strand (e), and random coil (c) structures in the four proteins. b The 3-D structures were predicted by the I-TASSER server (https://zhanglab.ccmb.med.umich.edu/I-TASSER/). Models of the 3D structures were modified using PyLOM software. Ribbon representations of the possible 3-D structures of four Hpa1 from three different views. Helical motifs are highlighted in red, while loop and turn motifs are highlighted in green. Sheet motifs are highlighted in yellow. Residues involved in the CC motifs are highlighted in blue. The two numbers ‘1’ and ‘2’ represent two stretches. Stretch 1 is a predicted α-helical region at the N-terminus; stretch 2 is a predicted α-helical region at the C-terminus